PMID- 16513177
OWN - NLM
STAT- MEDLINE
DCOM- 20060816
LR  - 20220311
IS  - 0162-0134 (Print)
IS  - 0162-0134 (Linking)
VI  - 100
IP  - 4
DP  - 2006 Apr
TI  - Stalking intermediates in oxygen activation by iron enzymes: motivation and 
      method.
PG  - 586-605
AB  - The study of high-valent-iron enzyme intermediates began in the mid-1900s with 
      the discovery of compounds I (or ES) and II in the heme peroxidases, progressed 
      to non-heme-diiron enzymes in the 1990s with the detection and characterization 
      of the Fe(III)-Fe(IV) complex, X, and the Fe(IV)-Fe(IV) complex, Q, in O(2) 
      activation by ribonucleotide reductase R2 (RNR-R2) and soluble methane 
      monooxygenase (sMMO), respectively, and was most recently extended to mononuclear 
      non-heme-iron oxygenases with the trapping and spectroscopic characterization of 
      the Fe(IV)-oxo intermediate, J, in the reaction of taurine:alpha-ketoglutarate 
      dioxygenase (TauD). Individually, each of these landmark studies helped reveal 
      the chemical logic of that particular enzyme system. Collectively, they have 
      significantly advanced our understanding of Nature's strategies for oxidative 
      transformation of biomolecules (both natural and "xenobiotic"). With high-valent 
      complexes now having been described in representatives of three major classes of 
      iron enzymes, it is an appropriate time to ask whether and what additional 
      insights might be gleaned from further stalking of related intermediates in other 
      systems. In this review, we advocate that there is still much to be learned from 
      this pursuit and summarize the insight provided by two of the landmark 
      discoveries mentioned above (the latter two) and the subsequent studies that they 
      spurred to support our contention. In addition, we attempt to provide, to the 
      extent that it is possible to do so, a "how-to" guide for detection and 
      characterization of such intermediates, focusing primarily on enzymes in which 
      they form by activation of molecular oxygen. In this latter objective, we have 
      drawn from an earlier review by Johnson (Enzymes, third ed. vol. 20, 1992, pp. 
      1-61) covering, more generally, dissection of enzyme reaction pathways by 
      transient-state kinetic methods. That work elegantly illustrated that, although 
      it may be impossible to develop a true algorithm for the process, a synthesis of 
      guidelines and general principles can be of considerable value.
FAU - Bollinger, J Martin Jr
AU  - Bollinger JM Jr
AD  - Department of Biochemistry and Molecular Biology, The Pennsylvania State 
      University, 306 South Frear Building, University Park, PA 16802, USA. 
      jmb21@psu.edu
FAU - Krebs, Carsten
AU  - Krebs C
LA  - eng
GR  - R01 GM069657/GM/NIGMS NIH HHS/United States
GR  - GM 55365/GM/NIGMS NIH HHS/United States
GR  - GM 69657/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20060302
PL  - United States
TA  - J Inorg Biochem
JT  - Journal of inorganic biochemistry
JID - 7905788
RN  - 0 (Enzymes)
RN  - 0 (Ferrous Compounds)
RN  - 0 (Iron-Binding Proteins)
RN  - 0 (Nonheme Iron Proteins)
RN  - 14127-53-8 (ferryl iron)
RN  - E1UOL152H7 (Iron)
RN  - EC 1.- (Mixed Function Oxygenases)
RN  - EC 1.14.11.- (taurine-alpha-ketoglutarate dioxygenase)
RN  - S88TT14065 (Oxygen)
SB  - IM
MH  - Enzymes/*chemistry
MH  - Ferrous Compounds/chemistry/metabolism
MH  - Iron/*chemistry/metabolism
MH  - Iron-Binding Proteins/*chemistry
MH  - Kinetics
MH  - Mixed Function Oxygenases/chemistry/metabolism
MH  - Nonheme Iron Proteins/chemistry/metabolism
MH  - Oxygen/*chemistry/metabolism
RF  - 117
EDAT- 2006/03/04 09:00
MHDA- 2006/08/17 09:00
CRDT- 2006/03/04 09:00
PHST- 2006/01/16 00:00 [received]
PHST- 2006/01/16 00:00 [accepted]
PHST- 2006/03/04 09:00 [pubmed]
PHST- 2006/08/17 09:00 [medline]
PHST- 2006/03/04 09:00 [entrez]
AID - S0162-0134(06)00028-6 [pii]
AID - 10.1016/j.jinorgbio.2006.01.022 [doi]
PST - ppublish
SO  - J Inorg Biochem. 2006 Apr;100(4):586-605. doi: 10.1016/j.jinorgbio.2006.01.022. 
      Epub 2006 Mar 2.